Association of Flavin Adenine Dinucleotide with the
            <i>Arabidopsis</i>
            Blue Light Receptor CRY1

Lin, Chentao; Robertson, Dan E.; Ahmad, Margaret; Raibekas, Andrei A.; Jörns, Marilyn Schuman; Dutton, P. Leslie; Cashmore, Anthony R.

doi:10.1126/science.7638620

Cited by 410 publications

(406 citation statements)

References 22 publications

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“…Because of the high sequence and structural similarities between photolyase and CRY, it is generally assumed that CRYs have the same two cofactors as well. However, no CRY has been purified to date from its native source and those that have been purified as recombinant proteins contain FAD to varying levels and either trace amounts of MTHF or none at all (Lin et al 1995;Malhotra et al 1995;Özgür and Sancar 2003;Song et al 2007). Hence, formal proof that CRYs contain MTHF, or any other secondary chromophore, is lacking.…”

Section: Structures Of Photolyase and Cryptochromementioning

confidence: 99%

“…Human cells expressing both genes and recombinant proteins encoded by both genes were tested for CPD and (6-4) photolyase activities and were found to lack both. Moreover, the proteins encoded by these genes, like most photolyases (Johnson et al 1988) and Arabidopsis CRY (Lin et al 1995;Malhorta et al 1995), contained FAD (flavin-adenine dinucleotide) and a pterin cofactor. Therefore, it was concluded that these proteins were not repair enzymes but that, like Arabidopsis CRYs, they performed non-repair-related blue light functions and were named human CRY1 and 2 (Hsu et al 1996).…”

Section: Historical Perspectivementioning

confidence: 99%

“…in response to blue light (Koornneef et al 1980), was isolated and sequenced, it revealed high sequence homology with Escherichia coli photolyase, and hence, it was in retrospect, correctly speculated that HY4 encoded a blue light photoreceptor and not a signal transducer involved in blue light response (Ahmad and Cashmore 1993). Later, this protein was named cryptochrome 1 (Lin et al 1995, and a second Arabidopsis protein that has high homology with CRY1 identified by genomics was named CRY2 . The role of CRY in Arabidopsis growth (CRY1) and differentiation (CRY2) was well established by 1995 (see Guo et al 1998).…”

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confidence: 99%

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Structure and Function of Animal Cryptochromes

Öztürk

Song²,

Özgür³

et al. 2007

Cold Spring Harbor Symposia on Quantitative Biology

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Cryptochrome (CRY) is a photolyase-like flavoprotein with no DNA-repair activity but with known or presumed blue-light receptor function. Animal CRYs have DNA-binding and autokinase activities, and their flavin cofactor is reduced by photoinduced electron transfer. In Drosophila, CRY is a major circadian photoreceptor, and in mammals, the two CRY proteins are core components of the molecular clock and potential circadian photoreceptors. In mammals, CRYs participate in cell cycle regulation and the cellular response to DNA damage by controlling the expression of some cell cycle genes and by directly interacting with checkpoint proteins. in response to blue light (Koornneef et al. 1980), was isolated and sequenced, it revealed high sequence homology with Escherichia coli photolyase, and hence, it was in retrospect, correctly speculated that HY4 encoded a blue light photoreceptor and not a signal transducer involved in blue light response (Ahmad and Cashmore 1993). Later, this protein was named cryptochrome 1 (Lin et al. 1995, and a second Arabidopsis protein that has high homology with CRY1 identified by genomics was named CRY2 . The role of CRY in Arabidopsis growth (CRY1) and differentiation (CRY2) was well established by 1995 (see Guo et al. 1998). However, as late as 1997, it was thought that CRY had no role in circadian photoreception in plants (Millar and Kay 1997).The first report implicating CRY in the circadian clock of any organism, plant or animal, came about from the study of DNA repair, in particular, the repair of UV damage in humans by photolyase. This issue had been controversial for nearly 25 years when Li et al. (1993) conducted an exhaustive study with a highly specific and sensitive assay, concluding that humans, like all placental mammals, lacked photolyase (Li et al. 1993). However, a 1995 release of a human expressed sequence tag (EST) list contained a "photolyase ortholog" entry (Adams et al. 1995). In light of this finding and the discovery of a photolyase in Drosophila and rattlesnake (Todo et al. 1993Kim et al. 1996) that repairs the minor UV-induced lesion, the (6-4) photoproduct, in contrast to the classic photolyase that repairs cyclobutane pyrimidine dimers (CPDs), the earlier conclusion regarding the lack of photolyase in humans needed reevaluation. This was done by Hsu et al. (1996) who, in addition to the "photolyase ortholog" in public databases, discovered a second human photolyase gene. Human cells expressing both genes and recombinant proteins encoded by both genes were tested for CPD and (6-4) photolyase activities and were found to lack both. Moreover, the proteins encoded by these genes, like most photolyases (Johnson et al. 1988) and Arabidopsis CRY (Lin et al. 1995; Malhorta et al. 1995), contained FAD (flavin-adenine dinucleotide) and a pterin cofactor. Therefore, it was concluded that these proteins were not repair enzymes but that, like Arabidopsis CRYs, they performed non-repair-related blue light functions and were named human CRY1 and 2 (Hsu et al. 1996). In humans ...

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Section: Structures Of Photolyase and Cryptochromementioning

confidence: 99%

Section: Historical Perspectivementioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Structure and Function of Animal Cryptochromes

Öztürk

Song²,

Özgür³

et al. 2007

Cold Spring Harbor Symposia on Quantitative Biology

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“…As is the case for phototropism in Arabidopsis, suppression of hypocotyl elongation in this species shows some sensitivity in the green. In this latter case, the most likely explanation is that the FAD in CRYl © 1997 Blackwell Science Ltd, Plant, Cell and Environment, 20, 768-772 can exist stably in a semiquinone form (Lin et al 1995b), a moiety with significant absoiption in the green portion of the visible spectrum. Since the evidence cited above supports the hypothesis that the photoreceptor for phototropism is a dual chromophore protein, the model seems reasonable.…”

Section: Future Prospectsmentioning

confidence: 99%

“…Ahmad & Cashmore (1993) described the isolation and characterization of an Arabidopsis gene, HY4, that probably encoded the photoreceptor for blue light-induced suppression of hypocotyl elongation. Subsequent biochemical studies (Lin et al 1995b) and investigations with transgenie plants overexpressing the HY4 gene product CRYl (Lin etal. 1995a) have confirmed this conclusion.…”

Section: Enter Arabidopsismentioning

confidence: 99%

The role of mutants in the search for the photoreceptor for phototropism in higher plants

Briggs¹,

Liscum²

1997

Plant Cell & Environment

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Early attempts to identify the chromophore of the photoreceptor for phototropism are reviewed. Carotenoids and flavins were the principal candidates, but studies with grass coleoptiles devoid of carotenoids suggest that at least in these organs carotenoids are most unlikely to play that role. The status of characterization of a gene for a putative photoreceptor protein is also reviewed. As the action spectrum for phototropism resembles the absorption spectrum of a flavoprotein, flavoproteins are attractive candidates at present, especially since the CRYl photoreceptor in Arabidopsis thaliana that mediates blue light-dependent hypocotyl growth suppression has flavin adenine dinucleotide as one of its two chromophores. As the second chromophore appears to be pterin, pterins should not be ruled out as candidate chromophores for the photoreceptor for phototropism.

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